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Zinc in PDB 4f04: A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound

Enzymatic activity of A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound

All present enzymatic activity of A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound:
2.1.3.2;

Protein crystallography data

The structure of A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound, PDB code: 4f04 was solved by A.W.Peterson, G.M.Cockrell, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.74 / 2.30
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.277, 121.277, 155.109, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 20.7

Zinc Binding Sites:

The binding sites of Zinc atom in the A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound (pdb code 4f04). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound, PDB code: 4f04:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4f04

Go back to Zinc Binding Sites List in 4f04
Zinc binding site 1 out of 2 in the A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:49.1
occ:1.00
SG B:CYS141 2.4 48.3 1.0
SG B:CYS109 2.4 50.7 1.0
SG B:CYS138 2.5 44.4 1.0
SG B:CYS114 2.5 47.3 1.0
CB B:CYS138 3.1 38.3 1.0
CB B:CYS114 3.1 40.5 1.0
CB B:CYS109 3.3 54.9 1.0
CB B:CYS141 3.3 44.4 1.0
N B:CYS141 3.7 43.8 1.0
CA B:CYS141 4.1 44.0 1.0
OG B:SER116 4.4 45.5 1.0
CA B:CYS114 4.5 45.8 1.0
CA B:CYS138 4.6 47.3 1.0
CB B:ASN111 4.6 51.9 1.0
O B:HOH303 4.7 48.4 1.0
ND2 B:ASN111 4.7 46.3 1.0
CA B:CYS109 4.7 59.1 1.0
CB B:TYR140 4.8 43.3 1.0
C B:CYS141 4.9 40.6 1.0
C B:TYR140 4.9 42.2 1.0
N B:GLU142 5.0 43.6 1.0

Zinc binding site 2 out of 2 in 4f04

Go back to Zinc Binding Sites List in 4f04
Zinc binding site 2 out of 2 in the A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Second Allosteric Site in E. Coli Aspartate Transcarbamoylase: R- State Atcase with Utp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn201

b:58.1
occ:1.00
SG D:CYS114 2.4 59.5 1.0
SG D:CYS109 2.5 63.6 1.0
SG D:CYS138 2.5 61.7 1.0
SG D:CYS141 2.5 61.2 1.0
CB D:CYS138 3.1 63.0 1.0
CB D:CYS114 3.2 61.3 1.0
CB D:CYS109 3.3 54.8 1.0
CB D:CYS141 3.3 52.4 1.0
N D:CYS141 3.7 56.3 1.0
CA D:CYS141 4.1 68.3 1.0
OG D:SER116 4.3 52.2 1.0
CA D:CYS114 4.5 56.9 1.0
CA D:CYS138 4.6 63.0 1.0
O D:HOH315 4.6 53.8 1.0
CB D:ASN111 4.7 68.0 1.0
CB D:TYR140 4.7 69.0 1.0
ND2 D:ASN111 4.7 57.5 1.0
CA D:CYS109 4.7 64.8 1.0
C D:TYR140 4.8 62.3 1.0
N D:TYR140 5.0 59.4 1.0

Reference:

A.W.Peterson, G.M.Cockrell, E.R.Kantrowitz. A Second Allosteric Site in Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 51 4776 2012.
ISSN: ISSN 0006-2960
PubMed: 22667327
DOI: 10.1021/BI3006219
Page generated: Sat Oct 26 22:11:51 2024

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